User:Jaime Prilusky/Test/references: Difference between revisions

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==test pdbe-citations for 3rec==

==test pdbe-citations for 8sbr==

== '''Overview''' ==

'''Phosphotriesterase-Like Lactonase (PLL)''' family includes a group of enzymes that have main lactonase activity on lactones and acyl-homoserin lactones (AHLs) and, in addition, low promiscuous phosphotriesterase activity towards organophosphates compound (OPs). At the beginning most of them has been identified as putative phosphotriesterases and were called "Paraoxonases" (Pox) because able to degrade pesticides such as paraoxon <ref>PMID: 15909078</ref> <ref>PMID:17337320</ref>. However, further structural, phylogenetic, and biochemical studies have revealed that these enzymes have a proficient lactonase activity, beside the weak phosphotriesterase activity <ref>PMID:17105187</ref>.

'''Phosphotriesterase-Like Lactonase (PLL)''' family includes a group of enzymes that have main lactonase activity on lactones and acyl-homoserin lactones (AHLs) and, in addition, low promiscuous phosphotriesterase activity towards organophosphates compound (OPs). At the beginning most of them has been identified as putative phosphotriesterases and were called "Paraoxonases" (Pox) because able to degrade pesticides such as paraoxon <ref name='Merone'>PMID: 15909078</ref> <ref name='Porzio'>PMID:17337320</ref>. However, further structural, phylogenetic, and biochemical studies have revealed that these enzymes have a proficient lactonase activity, beside the weak phosphotriesterase activity <ref name='Afriat'>PMID:17105187</ref>.

== '''SsoPox''' ==

Sso Pox is a protein of 314 aa deriving from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' and it is the first protein with phosphotriesterase activities to be identified in Archaea. It has an exceptional thermal stability with denaturation half-life of 4h and 90 min at 95 °C and 100 °C ~~(1) (2)~~.

Sso Pox is a protein of 314 aa deriving from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' and it is the first protein with phosphotriesterase activities to be identified in Archaea. It has an exceptional thermal stability with denaturation half-life of 4h and 90 min at 95 °C and 100 °C <ref name="Merone"/><ref name='Porzio'/>.

Its activity depends on the presence of metal ions, with cobalt significantly enhancing catalysis. SsoPox have been reported to catalyse the hydrolysis of different N-acyl homoserine lactones AHLs; suggesting a physiological role as a quorum quencher lactonase. Infact the AHLs are natural molecules involved in the cell–cell communication process known as quorum sensing (QS) and any bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain. The anti-QS mechanisms of the enzyme works by the hydrolysis of the lactone bond of these AHLs. ~~(3)~~

Its activity depends on the presence of metal ions, with cobalt significantly enhancing catalysis. SsoPox have been reported to catalyse the hydrolysis of different N-acyl homoserine lactones AHLs; suggesting a physiological role as a quorum quencher lactonase. Infact the AHLs are natural molecules involved in the cell–cell communication process known as quorum sensing (QS) and any bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain. The anti-QS mechanisms of the enzyme works by the hydrolysis of the lactone bond of these AHLs. <ref name='Afriat'/>

== References ==

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+==test pdbe-citations for 3rec==
+<div class="pdbe-citations 3rec" style="background-color:#fffaf0;"></div>
+==test pdbe-citations for 8sbr==
+<div class="pdbe-citations 8sbr" style="background-color:#fffaf0;"></div>
 == '''Overview''' ==
-'''Phosphotriesterase-Like Lactonase (PLL)''' family includes a group of enzymes that have main lactonase activity on lactones and acyl-homoserin lactones (AHLs) and, in addition, low promiscuous phosphotriesterase activity towards organophosphates compound (OPs). At the beginning most of them has been identified as putative phosphotriesterases and were called "Paraoxonases" (Pox) because able to degrade pesticides such as paraoxon <ref>PMID: 15909078</ref> <ref>PMID:17337320</ref>. However, further structural, phylogenetic, and biochemical studies have revealed that these enzymes have a proficient lactonase activity, beside the weak phosphotriesterase activity <ref>PMID:17105187</ref>.
+'''Phosphotriesterase-Like Lactonase (PLL)''' family includes a group of enzymes that have main lactonase activity on lactones and acyl-homoserin lactones (AHLs) and, in addition, low promiscuous phosphotriesterase activity towards organophosphates compound (OPs). At the beginning most of them has been identified as putative phosphotriesterases and were called "Paraoxonases" (Pox) because able to degrade pesticides such as paraoxon <ref name='Merone'>PMID: 15909078</ref> <ref name='Porzio'>PMID:17337320</ref>. However, further structural, phylogenetic, and biochemical studies have revealed that these enzymes have a proficient lactonase activity, beside the weak phosphotriesterase activity <ref name='Afriat'>PMID:17105187</ref>.
 == '''SsoPox''' ==
-Sso Pox is a protein of 314 aa deriving from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' and it is the first protein with phosphotriesterase activities to be identified in Archaea. It has an exceptional thermal stability with denaturation half-life of 4h and 90 min at 95 °C and 100 °C  (1) (2).
+Sso Pox is a protein of 314 aa deriving from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' and it is the first protein with phosphotriesterase activities to be identified in Archaea. It has an exceptional thermal stability with denaturation half-life of 4h and 90 min at 95 °C and 100 °C  <ref name="Merone"/><ref name='Porzio'/>.
-Its activity depends on the presence of metal ions, with cobalt significantly enhancing catalysis. SsoPox have been reported to catalyse the hydrolysis of different N-acyl homoserine lactones AHLs;  suggesting a physiological role as a quorum quencher lactonase. Infact the AHLs are natural molecules involved in the cell–cell communication process known as quorum sensing (QS) and any bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain. The anti-QS mechanisms of the enzyme works  by the hydrolysis of the lactone bond of these AHLs. (3)
+Its activity depends on the presence of metal ions, with cobalt significantly enhancing catalysis. SsoPox have been reported to catalyse the hydrolysis of different N-acyl homoserine lactones AHLs;  suggesting a physiological role as a quorum quencher lactonase. Infact the AHLs are natural molecules involved in the cell–cell communication process known as quorum sensing (QS) and any bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain. The anti-QS mechanisms of the enzyme works  by the hydrolysis of the lactone bond of these AHLs. <ref name='Afriat'/>
+== References ==
 <references/>